P24472 (GSTA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutathione S-transferase A4
EC=2.5.1.18

Alternative name(s):
GST A4-4
Short name=GSTA4-4
GST class-alpha member 4
Glutathione S-transferase 5.7
Short name=GST 5.7

Gene names

Name:	Gsta4
Synonyms:	Gsta

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	222 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Ref.6
Catalytic activity	RX + glutathione = HX + R-S-glutathione. Ref.6
Subunit structure	Homodimer. Ref.6
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	On the basis of immunological and kinetics data, GST 5.7 is distinct from alpha, mu and pI classes of GTS. However it has been postulated that this protein may be part of a distinct subgroup within this alpha class. The variations were found from AA sequencing and imply there are multiple forms of this protein. These variations are likely to be sex-linked and tissue specific.
Sequence similarities	Belongs to the GST superfamily. Alpha family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Molecular function	Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glutathione metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glutathione transferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 222

222

Glutathione S-transferase A4

PRO_0000185791

Regions

Domain

3 – 83

81

GST N-terminal

Domain

85 – 208

124

GST C-terminal

Region

54 – 55

2

Glutathione binding

Region

67 – 68

2

Glutathione binding

Sites

Binding site

9

1

Glutathione By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine By similarity

Natural variations

Natural variant

115

1

K → P Requires 2 nucleotide substitutions.

Natural variant

167

1

V → G.

Natural variant

179 – 180

2

PL → GE.

Experimental info

Sequence conflict

36

1

E → D in BAB31640. Ref.2

Sequence conflict

205 – 206

2

KP → SA in BAB27873. Ref.2

Sequence conflict

218

1

T → I in AAA37754. Ref.1

Secondary structure

1

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222

Helix Strand Turn

Details...

Beta strand

6 – 9

4

Turn

14 – 16

3

Helix

17 – 26

10

Beta strand

31 – 34

4

Helix

38 – 45

8

Turn

46 – 48

3

Beta strand

50 – 53

4

Beta strand

57 – 60

4

Beta strand

63 – 65

3

Helix

68 – 78

11

Helix

86 – 108

23

Helix

109 – 111

3

Helix

114 – 131

18

Helix

133 – 142

10

Beta strand

145 – 152

8

Helix

155 – 168

14

Helix

174 – 177

4

Helix

179 – 189

11

Helix

192 – 198

7

Beta strand

199 – 203

5

Helix

210 – 219

10

Sequences

	Sequence		Length	Mass (Da)
	P24472 [UniParc]. Last modified January 23, 2002. Version 3. Checksum: B580E3415289424D	FASTA	222	25,564
	10 20 30 40 50 60 MAAKPKLYYF NGRGRMESIR WLLAAAGVEF EEEFLETREQ YEKMQKDGHL LFGQVPLVEI 70 80 90 100 110 120 DGMMLTQTRA ILSYLAAKYN LYGKDLKERV RIDMYADGTQ DLMMMIAVAP FKTPKEKEES 130 140 150 160 170 180 YDLILSRAKT RYFPVFEKIL KDHGEAFLVG NQLSWADIQL LEAILMVEEL SAPVLSDFPL 190 200 210 220 LQAFKTRISN IPTIKKFLQP GSQRKPPPDG PYVEVVRTVL KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A subgroup of class alpha glutathione S-transferases. Cloning of cDNA for mouse lung glutathione S-transferase GST 5.7." Zimniak P., Eckles M.A., Saxena M., Awasthi Y.C. FEBS Lett. 313:173-176(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo, Small intestine and Tongue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Characterization of a novel glutathione S-transferase isoenzyme from mouse lung and liver having structural similarity to rat glutathione S-transferase 8-8." Medh R.D., Saxena M., Singhal S.S., Ahmad H., Awasthi Y.C. Biochem. J. 278:793-799(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 106-120 AND 167-184. Strain: CD-1. Tissue: Liver and Lung.
[5]	"Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress." Krengel U., Schroter K.H., Hoier H., Arkema A., Kalk K.H., Zimniak P., Dijkstra B.W. FEBS Lett. 422:285-290(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). Tissue: Lung.
[6]	"Crystal structure of a murine glutathione S-transferase in complex with a glutathione conjugate of 4-hydroxynon-2-enal in one subunit and glutathione in the other: evidence of signaling across the dimer interface." Xiao B., Singh S.P., Nanduri B., Awasthi Y.C., Zimniak P., Ji X. Biochemistry 38:11887-11894(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT. Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L06047 mRNA. Translation: AAA37754.1.
AK008189 mRNA. Translation: BAB25520.1.
AK008193 mRNA. Translation: BAB25524.1.
AK008400 mRNA. Translation: BAB25649.1.
AK008490 mRNA. Translation: BAB25696.1.
AK009668 mRNA. Translation: BAB26429.1.
AK010098 mRNA. Translation: BAB26701.1.
AK011177 mRNA. Translation: BAB27449.1.
AK011841 mRNA. Translation: BAB27873.1.
AK019100 mRNA. Translation: BAB31546.1.
AK019271 mRNA. Translation: BAB31640.1.
BC012639 mRNA. Translation: AAH12639.1.

IPI

IPI00323911.

PIR

S27234.

RefSeq

NP_034487.2. NM_010357.3.

UniGene

Mm.2662.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B48	X-ray	2.60	A/B	2-222	[»]
1GUK	X-ray	2.90	A/B	1-222	[»]

ProteinModelPortal

P24472.

SMR

P24472. Positions 2-222.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1487605.

PTM databases

PhosphoSite

P24472.

2D gel databases

REPRODUCTION-2DPAGE

P24472.

Proteomic databases

PaxDb

P24472.

PRIDE

P24472.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034903; ENSMUSP00000034903; ENSMUSG00000032348.

GeneID

14860.

KEGG

mmu:14860.

UCSC

uc009qty.2. mouse.

Organism-specific databases

CTD

2941.

MGI

MGI:1309515. Gsta4.

Phylogenomic databases

eggNOG

NOG266414.

GeneTree

ENSGT00670000097856.

HOGENOM

HOG000115734.

HOVERGEN

HBG053749.

InParanoid

P24472.

KO

K00799.

OMA

DLMGMIM.

OrthoDB

EOG4N5VXR.

Gene expression databases

Bgee

P24472.

CleanEx

MM_GSTA4.

Genevestigator

P24472.

GermOnline

ENSMUSG00000032348. Mus musculus.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR003080. GST_alpha.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

PANTHER

PTHR11571:SF4. PTHR11571:SF4. 1 hit.

Pfam

PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

PRINTS

PR01266. GSTRNSFRASEA.

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00143. Glutathione.

EvolutionaryTrace

P24472.

NextBio

287101.

SOURCE

Search...

Entry information

Entry name

GSTA4_MOUSE

Accession

Primary (citable) accession number: P24472
Secondary accession number(s): Q9CQ81 , Q9CTY7, Q9CY87, Q9D038

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	January 23, 2002
Last modified:	April 3, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program